Topological isomers of human uroguanylin: interconversion between biologically active and inactive isomers.
The solution structures of the two compounds of human uroguanylin (I and II), which were generated during disulfide bond forming reaction, were found to be topological isomers by 1H-nuclear magnetic resonance spectroscopy. These isomers are interconvertible in aqueous media at rates which vary with the pH and temperature of the solution. Because compound I is active in the cGMP producing assay, but compound II is not, this interconversion may be useful for evaluating the activity of human uroguanylin both in vivo and in vitro.
Chino
N
N
Peptide Institute, Inc., Protein Research Foundation, Minoh, Osaka, Japan. chino@prf.or.jp
Kubo
S
S
Kitani
T
T
Yoshida
T
T
Tanabe
R
R
Kobayashi
Y
Y
Nakazato
M
M
Kangawa
K
K
Kimura
T
T
D000595:Amino Acid Sequence; D000818:Animals; D005768:Gastrointestinal Hormones; D006801:Humans; D007536:Isomerism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D045265:Natriuretic Peptides; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry*; D011487:Protein Conformation; D051381:Rats; D016415:Sequence Alignment; D012996:Solutions
D005768:Gastrointestinal Hormones; D045265:Natriuretic Peptides; D010455:Peptides; D010456:Peptides, Cyclic; D012996:Solutions; C072685:guanylin; C084362:uroguanylin